ArticleThe Journal of biological chemistry2014
Structure and mechanism of mouse cyclase-associated protein (CAP1) in regulating actin dynamics.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 64 citations in OpenAlex.
- Mechanisms of disassembly at the actin filament pointed and barbed ends.Science advances · 2026Article
- The RCAR12-CAP1-OST1 module controls ABA-mediated stomatal closure in Arabidopsis.PLoS genetics · 2026Article
- CAP1-Mediated m6A modification of RRM2 suppresses tumor-associated M2 macrophage polarization and colorectal cancer growth.Cellular and molecular life sciences : CMLS · 2026Article
- The actin filament pointed-end depolymerase Srv2/CAP depolymerizes barbed ends, displaces capping protein, and promotes formin processivity.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Phalloidin and DNase I-bound F-actin pointed end structures reveal principles of filament stabilization and disassembly.Nature communications · 2024Article
- Multicomponent depolymerization of actin filament pointed ends by cofilin and cyclase-associated protein depends upon filament age.European journal of cell biology · 2024Article
- Multicomponent depolymerization of actin filament pointed ends by cofilin and cyclase-associated protein depends upon filament age.bioRxiv : the preprint server for biology · 2024Article
- Chemokine Receptor Antagonists Prevent and Reverse Cofilin-Actin Rod Pathology and Protect Synapses in Cultured Rodent and Human iPSC-Derived Neurons.Biomedicines · 2024Article
- Mechanisms of actin disassembly and turnover.The Journal of cell biology · 2023Review
- Cyclase-associated protein interacts with actin filament barbed ends to promote depolymerization and formin displacement.The Journal of biological chemistry · 2023Article
- Dynamic remodeling of actin networks by cyclase-associated protein and CAP-Abp1 complexes.Current biology : CB · 2023Article
- CAP1 (cyclase-associated protein 1) mediates the cyclic AMP signals that activate Rap1 in stimulating matrix adhesion of colon cancer cells.Cellular signalling · 2023Article
- Actomyosin-Driven Division of a Synthetic Cell.ACS synthetic biology · 2022Review
- Functional interdependence of the actin regulators CAP1 and cofilin1 in control of dendritic spine morphology.Cellular and molecular life sciences : CMLS · 2022Article
- Extensive identification of genes involved in congenital and structural heart disorders and cardiomyopathy.Nature cardiovascular research · 2022Article
- Review
- CAP1 binds and activates adenylyl cyclase in mammalian cells.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- CAP1, a target of miR-144/451, negatively regulates erythroid differentiation and enucleation.Journal of cellular and molecular medicine · 2021Article
- Cyclase-associated protein 2 (CAP2) controls MRTF-A localization and SRF activity in mouse embryonic fibroblasts.Scientific reports · 2021Article
- Twinfilin bypasses assembly conditions and actin filament aging to drive barbed end depolymerization.The Journal of cell biology · 2021Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Srv2/CAP is a conserved actin-binding protein with important roles in driving cellular actin dynamics in diverse animal, fungal, and plant species. However, there have been conflicting reports about whether the activities of Srv2/CAP are conserved, particularly between yeast and mammalian homologs. Yeast Srv2 has two distinct functions in actin turnover: its hexameric N-terminal-half enhances cofilin-mediated severing of filaments, while its C-terminal-half catalyzes dissociation of cofilin from ADP-actin monomers and stimulates nucleotide exchange. Here, we dissected the structure and function of mouse CAP1 to better understand its mechanistic relationship to yeast Srv2. Although CAP1 has a shorter N-terminal oligomerization sequence compared with Srv2, we find that the N-terminal-half of CAP1 (N-CAP1) forms hexameric structures with six protrusions, similar to N-Srv2. Further, N-CAP1 autonomously binds to F-actin and decorates the sides and ends of filaments, altering F-actin structure and enhancing cofilin-mediated severing. These activities depend on conserved surface residues on the helical-folded domain. Moreover, N-CAP1 enhances yeast cofilin-mediated severing, and conversely, yeast N-Srv2 enhances human cofilin-mediated severing, highlighting the mechanistic conservation between yeast and mammals. Further, we demonstrate that the C-terminal actin-binding β-sheet domain of CAP1 is sufficient to catalyze nucleotide-exchange of ADP-actin monomers, while in the presence of cofilin this activity additionally requires the WH2 domain. Thus, the structures, activities, and mechanisms of mouse and yeast Srv2/CAP homologs are remarkably well conserved, suggesting that the same activities and mechanisms underlie many of the diverse actin-based functions ascribed to Srv2/CAP homologs in different organisms.
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